Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ppGpp | ppGpp increases GldA activity with the half maximal activation at 33.1 microM | Escherichia coli |
Application | Comment | Organism |
---|---|---|
analysis | GldA shows a strong intrinsic fluorescence at 320 nm, when excited at 280 nm. The fluorescence intensity decreases in the presence of NAD+, NADH, and dihydroxyacetone, the substrate and products for GldA, which allows to determine the dissociation constants for those molecules as 110.6 microM, 9,1 microM, 33.3 mM, respectively | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
GDP | - |
Escherichia coli | |
GTP | - |
Escherichia coli | |
Tris(hydroxymethyl)aminomethane | competitive with respect to glycerol | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.22 | - |
NAD+ | pH 7.5, 25°C | Escherichia coli | |
48.9 | - |
glycerol | pH 7.5, 25°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A9S5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycerol + NAD+ | - |
Escherichia coli | glycerone + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GldA | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
12 | - |
- |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
10.6 | - |
GDP | pH 7.5, 25°C | Escherichia coli | |
16.1 | - |
GTP | pH 7.5, 25°C | Escherichia coli |